The AvrM effector from flax rust has a structured C-terminal domain and interacts directly with the M resistance protein.
Identifieur interne : 000147 ( Main/Corpus ); précédent : 000146; suivant : 000148The AvrM effector from flax rust has a structured C-terminal domain and interacts directly with the M resistance protein.
Auteurs : Ann-Maree Catanzariti ; Peter N. Dodds ; Thomas Ve ; Bostjan Kobe ; Jeffrey G. Ellis ; Brian J. StaskawiczSource :
- Molecular plant-microbe interactions : MPMI [ 0894-0282 ] ; 2010.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Amino Acids (genetics), Basidiomycota (genetics), Basidiomycota (metabolism), Basidiomycota (physiology), Cell Death (MeSH), Flax (genetics), Flax (metabolism), Flax (microbiology), Immunity, Innate (MeSH), Molecular Sequence Data (MeSH), Plant Diseases (microbiology), Plant Proteins (chemistry), Plant Proteins (metabolism), Polymorphism, Genetic (MeSH), Protein Binding (MeSH), Two-Hybrid System Techniques (MeSH).
- MESH :
- chemical , chemistry : Plant Proteins.
- chemical , genetics : Amino Acids.
- genetics : Basidiomycota, Flax.
- metabolism : Basidiomycota, Flax, Plant Proteins.
- microbiology : Flax, Plant Diseases.
- physiology : Basidiomycota.
- Amino Acid Sequence, Cell Death, Immunity, Innate, Molecular Sequence Data, Polymorphism, Genetic, Protein Binding, Two-Hybrid System Techniques.
Abstract
In plant immunity, recognition of pathogen effectors by plant resistance proteins leads to the activation of plant defenses and a localized cell death response. The AvrM effector from flax rust is a small secreted protein that is recognized by the M resistance protein in flax. Here, we investigate the mechanism of M-AvrM recognition and show that these two proteins directly interact in a yeast two-hybrid assay, and that this interaction correlates with the recognition specificity observed for each of the different AvrM variants. We further characterize this interaction by demonstrating that the C-terminal domain of AvrM is required for M-dependent cell death, and show that this domain also interacts with the M protein in yeast. We investigate the role of C-terminal differences among the different AvrM proteins for their involvement in this interaction and establish that M recognition is hindered by an additional 34 amino acids present at the C terminus of several AvrM variants. Structural characterization of recombinant AvrM-A protein revealed a globular C-terminal domain that dimerizes.
DOI: 10.1094/MPMI-23-1-0049
PubMed: 19958138
PubMed Central: PMC3142614
Links to Exploration step
pubmed:19958138Le document en format XML
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Dodds</name></author><author><name sortKey="Ve, Thomas" sort="Ve, Thomas" uniqKey="Ve T" first="Thomas" last="Ve">Thomas Ve</name></author><author><name sortKey="Kobe, Bostjan" sort="Kobe, Bostjan" uniqKey="Kobe B" first="Bostjan" last="Kobe">Bostjan Kobe</name></author><author><name sortKey="Ellis, Jeffrey G" sort="Ellis, Jeffrey G" uniqKey="Ellis J" first="Jeffrey G" last="Ellis">Jeffrey G. Ellis</name></author><author><name sortKey="Staskawicz, Brian J" sort="Staskawicz, Brian J" uniqKey="Staskawicz B" first="Brian J" last="Staskawicz">Brian J. Staskawicz</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2010">2010</date><idno type="RBID">pubmed:19958138</idno><idno type="pmid">19958138</idno><idno type="doi">10.1094/MPMI-23-1-0049</idno><idno type="pmc">PMC3142614</idno><idno type="wicri:Area/Main/Corpus">000147</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000147</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The AvrM effector from flax rust has a structured C-terminal domain and interacts directly with the M resistance protein.</title><author><name sortKey="Catanzariti, Ann Maree" sort="Catanzariti, Ann Maree" uniqKey="Catanzariti A" first="Ann-Maree" last="Catanzariti">Ann-Maree Catanzariti</name><affiliation><nlm:affiliation>Department of Plant and Microbial Biology, 111 Koshland Hall, University of California, Berkley 94720-3102, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Dodds, Peter N" sort="Dodds, Peter N" uniqKey="Dodds P" first="Peter N" last="Dodds">Peter N. Dodds</name></author><author><name sortKey="Ve, Thomas" sort="Ve, Thomas" uniqKey="Ve T" first="Thomas" last="Ve">Thomas Ve</name></author><author><name sortKey="Kobe, Bostjan" sort="Kobe, Bostjan" uniqKey="Kobe B" first="Bostjan" last="Kobe">Bostjan Kobe</name></author><author><name sortKey="Ellis, Jeffrey G" sort="Ellis, Jeffrey G" uniqKey="Ellis J" first="Jeffrey G" last="Ellis">Jeffrey G. Ellis</name></author><author><name sortKey="Staskawicz, Brian J" sort="Staskawicz, Brian J" uniqKey="Staskawicz B" first="Brian J" last="Staskawicz">Brian J. Staskawicz</name></author></analytic><series><title level="j">Molecular plant-microbe interactions : MPMI</title><idno type="ISSN">0894-0282</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Amino Acids (genetics)</term><term>Basidiomycota (genetics)</term><term>Basidiomycota (metabolism)</term><term>Basidiomycota (physiology)</term><term>Cell Death (MeSH)</term><term>Flax (genetics)</term><term>Flax (metabolism)</term><term>Flax (microbiology)</term><term>Immunity, Innate (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Plant Diseases (microbiology)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (metabolism)</term><term>Polymorphism, Genetic (MeSH)</term><term>Protein Binding (MeSH)</term><term>Two-Hybrid System Techniques (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Amino Acids</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Basidiomycota</term><term>Flax</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Basidiomycota</term><term>Flax</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Flax</term><term>Plant Diseases</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Cell Death</term><term>Immunity, Innate</term><term>Molecular Sequence Data</term><term>Polymorphism, Genetic</term><term>Protein Binding</term><term>Two-Hybrid System Techniques</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In plant immunity, recognition of pathogen effectors by plant resistance proteins leads to the activation of plant defenses and a localized cell death response. The AvrM effector from flax rust is a small secreted protein that is recognized by the M resistance protein in flax. Here, we investigate the mechanism of M-AvrM recognition and show that these two proteins directly interact in a yeast two-hybrid assay, and that this interaction correlates with the recognition specificity observed for each of the different AvrM variants. We further characterize this interaction by demonstrating that the C-terminal domain of AvrM is required for M-dependent cell death, and show that this domain also interacts with the M protein in yeast. We investigate the role of C-terminal differences among the different AvrM proteins for their involvement in this interaction and establish that M recognition is hindered by an additional 34 amino acids present at the C terminus of several AvrM variants. Structural characterization of recombinant AvrM-A protein revealed a globular C-terminal domain that dimerizes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19958138</PMID><DateCompleted><Year>2010</Year><Month>03</Month><Day>25</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0894-0282</ISSN><JournalIssue CitedMedium="Print"><Volume>23</Volume><Issue>1</Issue><PubDate><Year>2010</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Molecular plant-microbe interactions : MPMI</Title><ISOAbbreviation>Mol Plant Microbe Interact</ISOAbbreviation></Journal><ArticleTitle>The AvrM effector from flax rust has a structured C-terminal domain and interacts directly with the M resistance protein.</ArticleTitle><Pagination><MedlinePgn>49-57</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1094/MPMI-23-1-0049</ELocationID><Abstract><AbstractText>In plant immunity, recognition of pathogen effectors by plant resistance proteins leads to the activation of plant defenses and a localized cell death response. The AvrM effector from flax rust is a small secreted protein that is recognized by the M resistance protein in flax. Here, we investigate the mechanism of M-AvrM recognition and show that these two proteins directly interact in a yeast two-hybrid assay, and that this interaction correlates with the recognition specificity observed for each of the different AvrM variants. We further characterize this interaction by demonstrating that the C-terminal domain of AvrM is required for M-dependent cell death, and show that this domain also interacts with the M protein in yeast. We investigate the role of C-terminal differences among the different AvrM proteins for their involvement in this interaction and establish that M recognition is hindered by an additional 34 amino acids present at the C terminus of several AvrM variants. Structural characterization of recombinant AvrM-A protein revealed a globular C-terminal domain that dimerizes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Catanzariti</LastName><ForeName>Ann-Maree</ForeName><Initials>AM</Initials><AffiliationInfo><Affiliation>Department of Plant and Microbial Biology, 111 Koshland Hall, University of California, Berkley 94720-3102, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dodds</LastName><ForeName>Peter N</ForeName><Initials>PN</Initials></Author><Author ValidYN="Y"><LastName>Ve</LastName><ForeName>Thomas</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Kobe</LastName><ForeName>Bostjan</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Ellis</LastName><ForeName>Jeffrey G</ForeName><Initials>JG</Initials></Author><Author ValidYN="Y"><LastName>Staskawicz</LastName><ForeName>Brian J</ForeName><Initials>BJ</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM074265-01A2</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mol Plant Microbe Interact</MedlineTA><NlmUniqueID>9107902</NlmUniqueID><ISSNLinking>0894-0282</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid 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